4DAT

Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II

4DAT の概要

• エントリーDOI: 10.2210/pdb4dat/pdb
• 関連するPDBエントリー: 1YZ5 4DAU
• 分子名称: 14-3-3 protein sigma, Peptidylarginine Deiminase type VI, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: 14-3-3 fold, protein-protein interaction, signaling protein-protein binding complex, signaling protein/protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P31947
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27463.03

構造登録者

Rose, R.,Rose, M.,Ottmann, C. (登録日: 2012-01-13, 公開日: 2012-06-13, 最終更新日: 2024-10-30)

主引用文献

Rose, R.,Rose, M.,Ottmann, C.
Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI.
J.Struct.Biol., 180:65-72, 2012

PubMed Abstract: The regulation and function of peptidylarginine deiminase isoform VI (PAD6), which is a highly abundant protein associated with the cytoplasmic lattices in mammalian oocytes, is poorly understood so far. It has been shown previously, that 14-3-3 proteins, a class of regulatory adapter proteins ubiquitous in eukaryotes, bind to PAD6 in vivo in a phosphorylation dependent manner. Here we identify possible 14-3-3 binding sites in human PAD6 by in silico methods, looking for conserved, surface exposed serine residues. Two of these sites were confirmed as 14-3-3 binding sites by fluorescence polarization competition and X-ray crystallography. We furthermore suggest a role of RSK-type kinases in the phosphorylation of one of these two binding sites and provide evidence in the form of in vitro kinase assays with p70S6 kinase and RSK1.

PubMed: 22634725
DOI: 10.1016/j.jsb.2012.05.010

実験手法

X-RAY DIFFRACTION (1.4 Å)